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Protein

Alliin lyase 1

Gene
N/A
Organism
Allium sativum (Garlic)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Able to cleave the C-S bond of sulfoxide derivatives of Cys to produce allicin, thus giving rise to all sulfur compounds which are responsible for most of the properties of garlic, such as the specific smell and flavor as well as the health benefits like blood lipid or blood pressure lowering.

Catalytic activityi

An S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei132Chloride1
Binding sitei136Chloride1
Binding sitei138Chloride1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Chloride, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13504.

Names & Taxonomyi

Protein namesi
Recommended name:
Alliin lyase 1 (EC:4.4.1.4)
Short name:
Alliinase-1
Alternative name(s):
Cysteine sulphoxide lyase 1
OrganismiAllium sativum (Garlic)
Taxonomic identifieri4682 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAmaryllidaceaeAllioideaeAllieaeAllium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Protein family/group databases

Allergomei843. All s Alliin lyase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000002067729 – 381 Publication10
ChainiPRO_000002067839 – 486Alliin lyase 1Add BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi57N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi58 ↔ 77
Disulfide bondi79 ↔ 88
Disulfide bondi82 ↔ 95
Glycosylationi184N-linked (GlcNAc...)1
Glycosylationi229N-linked (GlcNAc...)Sequence analysis1
Modified residuei289N6-(pyridoxal phosphate)lysine1
Glycosylationi366N-linked (GlcNAc...)1
Disulfide bondi406 ↔ 414

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Bulb and shoots.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1486
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi44 – 54Combined sources11
Helixi59 – 61Combined sources3
Beta strandi83 – 85Combined sources3
Helixi105 – 107Combined sources3
Helixi108 – 111Combined sources4
Helixi115 – 118Combined sources4
Beta strandi120 – 122Combined sources3
Turni124 – 127Combined sources4
Beta strandi129 – 131Combined sources3
Helixi141 – 154Combined sources14
Beta strandi163 – 168Combined sources6
Helixi169 – 181Combined sources13
Turni185 – 187Combined sources3
Beta strandi194 – 198Combined sources5
Helixi204 – 212Combined sources9
Beta strandi218 – 223Combined sources6
Helixi224 – 227Combined sources4
Helixi233 – 235Combined sources3
Beta strandi236 – 243Combined sources8
Turni245 – 247Combined sources3
Beta strandi259 – 263Combined sources5
Turni269 – 271Combined sources3
Beta strandi281 – 286Combined sources6
Helixi287 – 290Combined sources4
Helixi294 – 296Combined sources3
Beta strandi299 – 303Combined sources5
Helixi306 – 319Combined sources14
Beta strandi320 – 322Combined sources3
Helixi325 – 345Combined sources21
Helixi352 – 371Combined sources20
Beta strandi374 – 378Combined sources5
Beta strandi386 – 388Combined sources3
Turni389 – 392Combined sources4
Beta strandi393 – 395Combined sources3
Beta strandi400 – 406Combined sources7
Helixi409 – 411Combined sources3
Helixi414 – 420Combined sources7
Helixi428 – 431Combined sources4
Beta strandi437 – 441Combined sources5
Helixi446 – 460Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LK9X-ray1.53A/B39-486[»]
2HORX-ray1.60A39-465[»]
2HOXX-ray1.40A/B/C/D39-465[»]
ProteinModelPortaliQ01594.
SMRiQ01594.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01594.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 97EGF-like; atypicalAdd BLAST47

Domaini

The 6 Cys residues of the EGF-like domain are arranged in a disulfide pattern different from the one found in the canonical EGFs. The function of this domain is unclear. It may be a binding site for other proteins or the docking site for a putative alliinase receptor.

Sequence similaritiesi

Belongs to the alliinase family.Curated
Contains 1 EGF-like domain.Curated

Keywords - Domaini

EGF-like domain, Signal

Family and domain databases

Gene3Di2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF04864. Alliinase_C. 1 hit.
PF04863. EGF_alliinase. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01594-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVESYKKIGS CNKMPCLVIL TCIIMSNSLV NNNNMVQAKM TWTMKAAEEA
60 70 80 90 100
EAVANINCSE HGRAFLDGII SEGSPKCECN TCYTGPDCSE KIQGCSADVA
110 120 130 140 150
SGDGLFLEEY WKQHKEASAV LVSPWHRMSY FFNPVSNFIS FELEKTIKEL
160 170 180 190 200
HEVVGNAAAK DRYIVFGVGV TQLIHGLVIS LSPNMTATPD APESKVVAHA
210 220 230 240 250
PFYPVFREQT KYFNKKGYVW AGNAANYVNV SNPEQYIEMV TSPNNPEGLL
260 270 280 290 300
RHAVIKGCKS IYDMVYYWPH YTPIKYKADE DILLFTMSKF TGHSGSRFGW
310 320 330 340 350
ALIKDESVYN NLLNYMTKNT EGTPRETQLR SLKVLKEVVA MVKTQKGTMR
360 370 380 390 400
DLNTFGFKKL RERWVNITAL LDQSDRFSYQ ELPQSEYCNY FRRMRPPSPS
410 420 430 440 450
YAWVKCEWEE DKDCYQTFQN GRINTQNGVG FEASSRYVRL SLIKTQDDFD
460 470 480
QLMYYLKDMV KAKRKTPLIK QLFIDQTETA SRRPFI
Length:486
Mass (Da):55,639
Last modified:July 1, 1993 - v1
Checksum:iD7862E867AD74383
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12622 mRNA. Translation: CAA78268.1.
PIRiS29302.

Cross-referencesi

Web resourcesi

Protein Spotlight

What's that smell? - Issue 39 of October 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12622 mRNA. Translation: CAA78268.1.
PIRiS29302.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LK9X-ray1.53A/B39-486[»]
2HORX-ray1.60A39-465[»]
2HOXX-ray1.40A/B/C/D39-465[»]
ProteinModelPortaliQ01594.
SMRiQ01594.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei843. All s Alliin lyase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13504.

Miscellaneous databases

EvolutionaryTraceiQ01594.

Family and domain databases

Gene3Di2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF04864. Alliinase_C. 1 hit.
PF04863. EGF_alliinase. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALLN1_ALLSA
AccessioniPrimary (citable) accession number: Q01594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.